5VC1

Crystal structure of L-selectin lectin/EGF domains

5VC1 の概要

• エントリーDOI: 10.2210/pdb5vc1/pdb
• 分子名称: L-selectin, beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, TETRAETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: l-selectin; glycoprotein, cell adhesion
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19756.02

構造登録者

Wedepohl, S.,Dernedde, J.,Vahedi-Faridi, A.,Tauber, R.,Saenger, W.,Bulut, H. (登録日: 2017-03-30, 公開日: 2017-06-14, 最終更新日: 2024-10-23)

主引用文献

Wedepohl, S.,Dernedde, J.,Vahedi-Faridi, A.,Tauber, R.,Saenger, W.,Bulut, H.
Reducing Macro- and Microheterogeneity of N-Glycans Enables the Crystal Structure of the Lectin and EGF-Like Domains of Human L-Selectin To Be Solved at 1.9 angstrom Resolution.
Chembiochem, 18:1338-1345, 2017

PubMed Abstract: L-Selectin, a cell-adhesion receptor on the surface of most leukocytes, contains seven N-glycosylation sites. In order to obtain the crystal structure of human L-selectin, we expressed a shortened version of L-selectin comprising the C-type lectin and EGF-like domains (termed LE) and systematically analysed mutations of the three glycosylation sites (Asn22, Asn66 and Asn139) in order to reduce macroheterogeneity. After we further removed microheterogeneity, we obtained crystals that diffracted X-rays up to 1.9 Å from a variant (LE010) with exchanges N22Q and N139Q and one GlcNAc Man N-glycan chain attached to Asn66. Crystal-structure analysis showed that the terminal mannose of GlcNAc Man of one LE010 molecule was coordinated to Ca in the binding site of a symmetry-related LE010. The orientation of the lectin and EGF-like domain was similar to the described "bent" conformation of E- and P-selectins. The Ca -binding site reflects the binding mode seen in E- and P-selectin structures co-crystallised with ligands.

PubMed: 28489325
DOI: 10.1002/cbic.201700220

実験手法

X-RAY DIFFRACTION (1.94 Å)